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Am J Physiol Cell Physiol 278: C500-C508, 2000;
0363-6143/00 $5.00
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Vol. 278, Issue 3, C500-C508, March 2000

ERK signaling mediates the induction of inflammatory cytokines by bufalin in human monocytic cells

Masahiro Kurosawa, Satoshi Numazawa, Yoshihiro Tani, and Takemi Yoshida

Department of Biochemical Toxicology, School of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, Japan

Treatment of human leukemia THP-1 cells with bufalin, a specific inhibitor of Na+-K+-ATPase, sequentially induces c-fos and inflammatory cytokines interleukin-1beta (IL-1beta ) and tumor necrosis factor-alpha (TNF-alpha ) gene expressions before the appearance of mature phenotypes of monocytic cells. In this study we examined the signal transduction leading to bufalin-induced gene expressions. Bufalin selectively activated extracellular signal-regulated kinase (ERK), compared with other mitogen-activated protein (MAP) kinase family members. Pretreatment of THP-1 cells with PD-98059, an inhibitor of the ERK-kinase cascade, abolished bufalin-induced c-fos and IL-1beta gene expressions, indicating that the ERK-kinase cascade mediates the induction of inflammatory cytokines by bufalin. Inhibition of the Na+/Ca2+ exchanger by KB-R7943 and of protein kinase C (PKC) by Ro-31-8220 suppressed ERK activation and gene expressions of c-fos and IL-1beta . These findings suggest that Na+-K+-ATPase inhibition by bufalin induces calcium influx and thereby activates PKC and ERK. In cells treated with an inhibitor of p38 MAP kinases, SB-203580, bufalin-mediated ERK activation became persistent and the induction of IL-1beta and TNF-alpha expressions was significantly augmented. These results suggest that cross talk in bufalin-mediated ERK activation is negatively regulated by endogenous p38 MAP kinase activations.

interleukin-1beta ; sodium-potassium-adenosinetriphosphatase; cell differentiation; extracellular signal-regulated kinase


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